Positional preferences in flavonoids for inhibition of ribonuclease A: Where “- OH ” where?

Tripathy, Debi Ranjan ; Panda, Atashi ; Dinda, Amit Kumar ; Dasgupta, Swagata (2021) Positional preferences in flavonoids for inhibition of ribonuclease A: Where “- OH ” where? Proteins: Structure, Function, and Bioinformatics, 89 (5). pp. 577-587. ISSN 0887-3585

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Official URL: http://doi.org/10.1002/prot.26043

Related URL: http://dx.doi.org/10.1002/prot.26043


Flavonoids are a class of polyphenols that possess diverse properties. The structure-activity relationship of certain flavonoids and resveratrol with ribonuclease A (RNase A) has been investigated. The selected flavonoids have a similar skeleton and the positional preferences of the phenolic moieties toward inhibition of the catalytic activity of RNase A have been studied. The results obtained for RNase A inhibition by flavonoids suggest that the planarity of the molecules is necessary for effective inhibitory potency. Agarose gel electrophoresis and precipitation assay experiments along with kinetic studies reveal Ki values for the various flavonoids in the micromolar range. Minor secondary structural changes of RNase A were observed after interaction with the flavonoids. An insight into the specific amino acid involvement in the binding of the substrate using docking studies is also presented. The dipole moment of the flavonoids that depends on the orientation of the hydroxyl groups in the molecule bears direct correlation with the inhibitory potency against RNase A. The direct association of this molecular property with enzyme inhibition can be exploited for the design and development of inhibitors of proteins.

Item Type:Article
Source:Copyright of this article belongs to John Wiley & Sons, Inc.
ID Code:123635
Deposited On:10 Oct 2021 08:49
Last Modified:10 Oct 2021 08:49

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